Investigation of functional mutants of yeast (Saccharomyces cerevisiae) alcohol dehydrogenase which are capable of altering the redox balance in the cell and are affected in binding constants and turnover number. Isolation of conditional mutants exhibiting similar properties, and of functional mutants resistant to specific inhibitors. Correlation of amino acid substitutions in these mutants with kinetic changes and with the tertiary structure of this enzyme. Eventual goal: developement of this enzyme system to the point where biochemical investigations as detailed as those carried out on hemoglobin are feasible. Health-related aspects: development of yeast alcohol dehydrogenase as a model for mammalian alcohol dehydrogenases, understanding of mechanisms of inhibition and the design of more efficient and precisely targeted inhibitors.